Vibrational Spectroscopic Studies on Fibrinogen Adsorption at Polystyrene/Protein Solution Interfaces:  Hydrophobic Side Chain and Secondary Structure Changes

2006 ◽  
Vol 110 (10) ◽  
pp. 5017-5024 ◽  
Author(s):  
Jie Wang ◽  
Xiaoyun Chen ◽  
Matthew L. Clarke ◽  
Zhan Chen
Keyword(s):  
Secondary Structure ◽  
Spectroscopic Studies ◽  
Side Chain ◽  
Protein Solution ◽  
Structure Changes ◽  
Fibrinogen Adsorption

FTIR Analysis of the Lignin Structure Changes of APMP Treated by Laccase and Laccase / Mediator System

2013 ◽  
Vol 734-737 ◽  
pp. 2089-2093
Author(s):  
Fan Liu ◽  
Yu Liu ◽  
Jia Chuan Chen ◽  
Zhen Wang
Keyword(s):  
Oxidative Degradation ◽  
No Oxidation ◽  
Side Chain ◽  
Content Increase ◽  
Hydroxyl Content ◽  
Structure Changes ◽  
Mediator System ◽  
Chromophoric Group ◽  
Laccase Mediator System ◽  
Lignin Structure

In this Paper the Two-Stage Method of Enzyme-Mild Acidic Hydrolysis was Adopted to Separate Lignin from the APMP and the Modified Pulp Samples.And then Analyze the Lignin Structure Changes of the Modified APMP Lignin by Laccase and LMS(laccase/mediator System). it was Found that no Oxidation Took Place on Carbohydrates in the LMS, and Lignin Cα Hydroxyl Oxidization Produce α Carbonyl and H2O2 Bleaching can also Oxidation of Lignin, make the Conjugate C = α Increase;the Syringyl Structure Hydroxyl Content Increase, the Lignin Structure Macromolecular Side Chain Fracturing; Laccase and LMS Oxidative Degradation Chromophoric Group Unsaturated C = O, which can Improve the Brightness of Pulp and Create Better Conditions for Unbleached Pulp.

Secondary structure of pig skin proteodermatan sulfate: A perspective from Raman spectroscopic studies in aqueous solution

Biopolymers ◽  
1989 ◽  
Vol 28 (11) ◽  
pp. 1935-1938 ◽  
Author(s):  
V. Renugopalakrishnan ◽  
S. Zheng ◽  
A. T. Tu ◽  
S. P. Damle
Keyword(s):  
Aqueous Solution ◽  
Secondary Structure ◽  
Spectroscopic Studies ◽  
Raman Spectroscopic ◽  
Pig Skin

scholarly journals Systematic FTIR Spectroscopy Study of the Secondary Structure Changes in Human Serum Albumin under Various Denaturation Conditions

Biomolecules ◽  
2019 ◽  
Vol 9 (8) ◽  
pp. 359 ◽  
Author(s):  
Usoltsev ◽  
Sitnikova ◽  
Kajava ◽  
Uspenskaya
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Ftir Spectroscopy ◽  
Conformational Changes ◽  
Data Interpretation ◽  
Random Coil ◽  
Helical Conformation ◽  
Structure Changes

Human serum albumin (HSA) is the most abundant protein in blood plasma. HSA is involved in the transport of hormones, fatty acids, and some other compounds, maintenance of blood pH, osmotic pressure, and many other functions. Although this protein is well studied, data about its conformational changes upon different denaturation factors are fragmentary and sometimes contradictory. This is especially true for FTIR spectroscopy data interpretation. Here, the effect of various denaturing agents on the structural state of HSA by using FTIR spectroscopy in the aqueous solutions was systematically studied. Our data suggest that the second derivative deconvolution method provides the most consistent interpretation of the obtained IR spectra. The secondary structure changes of HSA were studied depending on the concentration of the denaturing agent during acid, alkaline, and thermal denaturation. In general, the denaturation of HSA in different conditions is accompanied by a decrease in α-helical conformation and an increase in random coil conformation and the intermolecular β-strands. Meantime, some variation in the conformational changes depending on the type of the denaturation agent were also observed. The increase of β-structural conformation suggests that HSA may form amyloid-like aggregates upon the denaturation.

scholarly journals Does the conformation of adsorbed fibrinogen dictate platelet interactions with artificial surfaces?

Blood ◽  
1986 ◽  
Vol 68 (2) ◽  
pp. 355-362 ◽  
Author(s):  
JN Lindon ◽  
G McManama ◽  
L Kushner ◽  
EW Merrill ◽  
EW Salzman
Keyword(s):  
Platelet Adhesion ◽  
Surface Coverage ◽  
Platelet Reactivity ◽  
Polymer Surfaces ◽  
Side Chain ◽  
Alkyl Side Chain ◽  
Fibrinogen Binding ◽  
Artificial Surfaces ◽  
Antibody Preparations ◽  
Fibrinogen Adsorption

Abstract Platelet activation by polymer surfaces is thought to require preliminary adsorption of fibrinogen and perhaps changes in fibrinogen conformation. We measured fibrinogen adsorption by a series of polymers by two methods, using either 125I-labeled fibrinogen or 125I-labeled antifibrinogen antibodies, and correlated the results with platelet reactivity (retention and secretion) in columns of beads coated with the polymers. For polyalkyl methacrylates with 1 to 4 carbon side chains, platelet reactivity varied directly with increasing length of the alkyl side chain and with the quantity of bound fibrinogen recognizable by antifibrinogen antibody but not with the total quantity of fibrinogen adsorbed. The same pattern of results was seen with five antibody preparations, including affinity-purified Fab fragments against the D or E domain of fibrinogen. Tests of platelet retention and fibrinogen binding to four polyalkyl acrylates and to three unrelated polymers (polystyrene, polymethyl methacrylate, and a polyether polyurethane) indicated that platelet retention correlated positively with both total fibrinogen binding and with the amount of antibody-recognizable fibrinogen bound. Drugs that block platelet aggregation, but not adhesion, did not alter the hierarchy of platelet retention to the polyalkyl methacrylates. These data suggest that, contrary to previous views, platelet adhesion to artificial surfaces increases with increasing surface coverage of adsorbed fibrinogen if the bound fibrinogen maintains a conformation such that its functional domains remain recognizable by antibody probes.

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